ID   PALY_AGABI              Reviewed;         142 AA.
AC   Q92195;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Phenylalanine ammonia-lyase {ECO:0000303|Ref.1};
DE            EC=4.3.1.24 {ECO:0000250|UniProtKB:A0A4Y6HUI7};
DE   Flags: Fragment;
GN   Name=palA;
OS   Agaricus bisporus (White button mushroom).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricaceae; Agaricus.
OX   NCBI_TaxID=5341;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Horst U1;
RA   Basten D.E.J.W., de Groot P.W.J., Schaap P.J., Visser J.;
RT   "cDNA fragment of the gene encoding phenylalanine ammonia-lyase from
RT   Agaricus bisporus.";
RL   Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the non-oxidative deamination of L-phenylalanine to
CC       form trans-cinnamic acid and a free ammonium ion (By similarity).
CC       Facilitates the commitment step in phenylpropanoid pathways that
CC       produce secondary metabolites such as lignins, coumarins and flavonoids
CC       (By similarity). {ECO:0000250|UniProtKB:A0A4Y6HUI7,
CC       ECO:0000250|UniProtKB:P11544}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-phenylalanine = (E)-cinnamate + NH4(+);
CC         Xref=Rhea:RHEA:21384, ChEBI:CHEBI:15669, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:58095; EC=4.3.1.24;
CC         Evidence={ECO:0000250|UniProtKB:A0A4Y6HUI7};
CC   -!- PATHWAY: Phenylpropanoid metabolism; trans-cinnamate biosynthesis;
CC       trans-cinnamate from L-phenylalanine: step 1/1. {ECO:0000305}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P11544}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which
CC       is formed autocatalytically by cyclization and dehydration of residues
CC       Ala-Ser-Gly. {ECO:0000250|UniProtKB:Q68G84}.
CC   -!- SIMILARITY: Belongs to the PAL/histidase family. {ECO:0000305}.
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DR   EMBL; Z82018; CAB04783.1; -; mRNA.
DR   AlphaFoldDB; Q92195; -.
DR   SMR; Q92195; -.
DR   UniPathway; UPA00713; UER00725.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0045548; F:phenylalanine ammonia-lyase activity; ISS:UniProtKB.
DR   GO; GO:0009800; P:cinnamic acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001106; Aromatic_Lyase.
DR   InterPro; IPR008948; L-Aspartase-like.
DR   PANTHER; PTHR10362; PTHR10362; 1.
DR   Pfam; PF00221; Lyase_aromatic; 1.
DR   SUPFAM; SSF48557; SSF48557; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Lyase; Phenylalanine catabolism; Phenylpropanoid metabolism.
FT   CHAIN           <1..>142
FT                   /note="Phenylalanine ammonia-lyase"
FT                   /id="PRO_0000215429"
FT   BINDING         97
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   NON_TER         1
FT   NON_TER         142
SQ   SEQUENCE   142 AA;  15200 MW;  93F82EAAD1E4C7F9 CRC64;
     ETGRIHHGGN FQAMAVTNAM EKTRLALHHI GKIIFAQSTE LINPATNRGL PPSLAASDPS
     LNYHVKGVDI ATAAYAAELG YLASPVSTHI QSAEMHNQAV NSMALVSARA TINSIDVLSM
     LVATYLYNLC QALDLRALQA EF